2.360 Å
X-ray
2009-05-07
Name: | UDP-galactopyranose mutase |
---|---|
ID: | Q9RYF1_DEIRA |
AC: | Q9RYF1 |
Organism: | Deinococcus radiodurans |
Reign: | Bacteria |
TaxID: | 243230 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 29.270 |
---|---|
Number of residues: | 45 |
Including | |
Standard Amino Acids: | 42 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 2 |
Cofactors: | FAD |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.236 | 705.375 |
% Hydrophobic | % Polar |
---|---|
35.89 | 64.11 |
According to VolSite |
HET Code: | GDU |
---|---|
Formula: | C15H22N2O17P2 |
Molecular weight: | 564.286 g/mol |
DrugBank ID: | DB03501 |
Buried Surface Area: | 77 % |
Polar Surface area: | 316.82 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 7 |
Rings: | 3 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 9 |
X | Y | Z |
---|---|---|
24.1245 | -106.259 | 73.4552 |
Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand
Ligand | Protein | Interaction | |||
---|---|---|---|---|---|
Atom | Atom | Residue | Distance (Å) | Angle (°) | Type |
C6' | CG | PRO- 84 | 3.81 | 0 | Hydrophobic |
C6' | CD1 | ILE- 86 | 3.79 | 0 | Hydrophobic |
O6' | NE2 | HIS- 109 | 3.18 | 152.11 | H-Bond (Protein Donor) |
N3 | O | PHE- 175 | 2.94 | 153.72 | H-Bond (Ligand Donor) |
C1D | CD1 | PHE- 176 | 3.94 | 0 | Hydrophobic |
C3D | CE2 | TYR- 179 | 3.9 | 0 | Hydrophobic |
C2D | CD2 | TYR- 179 | 3.68 | 0 | Hydrophobic |
C2D | CB | THR- 180 | 4.47 | 0 | Hydrophobic |
O2D | OG1 | THR- 180 | 3 | 162.8 | H-Bond (Ligand Donor) |
O3D | NE1 | TRP- 184 | 3.02 | 144.17 | H-Bond (Protein Donor) |
C4D | CG1 | VAL- 195 | 4.03 | 0 | Hydrophobic |
C1D | CG2 | THR- 196 | 4.28 | 0 | Hydrophobic |
C5D | CD | ARG- 198 | 3.74 | 0 | Hydrophobic |
O2A | NE | ARG- 198 | 2.87 | 153.15 | H-Bond (Protein Donor) |
O2A | NH2 | ARG- 198 | 3.04 | 140.45 | H-Bond (Protein Donor) |
O2A | CZ | ARG- 198 | 3.37 | 0 | Ionic (Protein Cationic) |
C5D | CG2 | VAL- 199 | 4.34 | 0 | Hydrophobic |
C4' | CE2 | TYR- 209 | 3.87 | 0 | Hydrophobic |
C4' | CZ | PHE- 210 | 3.76 | 0 | Hydrophobic |
O6' | OG1 | THR- 294 | 3.31 | 154.68 | H-Bond (Protein Donor) |
O4 | ND2 | ASN- 296 | 3.07 | 152.6 | H-Bond (Protein Donor) |
O1B | NH2 | ARG- 305 | 3.3 | 127.25 | H-Bond (Protein Donor) |
O3B | NH2 | ARG- 305 | 3.43 | 133.32 | H-Bond (Protein Donor) |
O3B | NH1 | ARG- 305 | 2.85 | 167.09 | H-Bond (Protein Donor) |
O1B | CZ | ARG- 305 | 3.8 | 0 | Ionic (Protein Cationic) |
O1B | OH | TYR- 335 | 2.83 | 151.15 | H-Bond (Protein Donor) |
O2B | OH | TYR- 370 | 2.77 | 160.1 | H-Bond (Protein Donor) |
O6' | O | HOH- 448 | 2.79 | 144.77 | H-Bond (Ligand Donor) |
C1' | C6 | FAD- 450 | 3.77 | 0 | Hydrophobic |
O4' | O4 | FAD- 450 | 2.8 | 133.36 | H-Bond (Ligand Donor) |